5NER

Localised reconstruction of alpha v beta 6 bound to Foot and Mouth Disease Virus O PanAsia - Pose A prime.

5NER の概要

• エントリーDOI: 10.2210/pdb5ner/pdb
• EMDBエントリー: 3630 3632 3633
• 関連するBIRD辞書のPRD_ID: PRD_900111
• 分子名称: O PanAsia VP1, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (14 entities in total)
• 機能のキーワード: foot and mouth disease virus, fmdv, virus, opanasia, virus-receptor, complex
• 由来する生物種: Foot-and-mouth disease virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 199928.29

構造登録者

Kotecha, A.,Stuart, D. (登録日: 2017-03-11, 公開日: 2017-06-21, 最終更新日: 2024-10-23)

主引用文献

Kotecha, A.,Wang, Q.,Dong, X.,Ilca, S.L.,Ondiviela, M.,Zihe, R.,Seago, J.,Charleston, B.,Fry, E.E.,Abrescia, N.G.A.,Springer, T.A.,Huiskonen, J.T.,Stuart, D.I.
Rules of engagement between alpha v beta 6 integrin and foot-and-mouth disease virus.
Nat Commun, 8:15408-15408, 2017

PubMed Abstract: Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally αvβ6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between αvβ6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role.

PubMed: 28534487
DOI: 10.1038/ncomms15408

実験手法

ELECTRON MICROSCOPY (11.5 Å)